Structural basis for arabinoxylo-oligosaccharide capture by the probiotic Bifidobacterium animalis subsp lactis Bl-04
(2012) In Journal of Psychopharmacology 26(11). p.1100-1112- Abstract
- Glycan utilization plays a key role in modulating the composition of the gut microbiota, but molecular insight into oligosaccharide uptake by this microbial community is lacking. Arabinoxylo-oligosaccharides (AXOS) are abundant in the diet, and are selectively fermented by probiotic bifidobacteria in the colon. Here we show how selectivity for AXOS uptake is established by the probiotic strain Bifidobacterium animalis subsp. lactisBl-04. The binding protein BlAXBP, which is associated with an ATP-binding cassette (ABC) transporter that mediates the uptake of AXOS, displays an exceptionally broad specificity for arabinosyl-decorated and undecorated xylo-oligosaccharides, with preference for tri- and tetra-saccharides. Crystal structures of... (More)
- Glycan utilization plays a key role in modulating the composition of the gut microbiota, but molecular insight into oligosaccharide uptake by this microbial community is lacking. Arabinoxylo-oligosaccharides (AXOS) are abundant in the diet, and are selectively fermented by probiotic bifidobacteria in the colon. Here we show how selectivity for AXOS uptake is established by the probiotic strain Bifidobacterium animalis subsp. lactisBl-04. The binding protein BlAXBP, which is associated with an ATP-binding cassette (ABC) transporter that mediates the uptake of AXOS, displays an exceptionally broad specificity for arabinosyl-decorated and undecorated xylo-oligosaccharides, with preference for tri- and tetra-saccharides. Crystal structures of BlAXBP in complex with four different ligands revealed the basis for this versatility. Uniquely, the protein was able to recognize oligosaccharides in two opposite orientations, which facilitates the optimization of interactions with the various ligands. Broad substrate specificity was further enhanced by a spacious binding pocket accommodating decorations at different mainchain positions and conformational flexibility of a lid-like loop. Phylogenetic and genetic analyses show that BlAXBP is highly conserved within Bifidobacterium, but is lacking in other gut microbiota members. These data indicate niche adaptation within Bifidobacterium and highlight the metabolic syntrophy (cross-feeding) among the gut microbiota. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4275397
- author
- Ejby, Morten ; Fredslund, Folmer LU ; Vujicic-Zagar, Andreja ; Svensson, Birte ; Slotboom, Dirk Jan and Abou Hachem, Maher
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Psychopharmacology
- volume
- 26
- issue
- 11
- pages
- 1100 - 1112
- publisher
- SAGE Publications
- external identifiers
-
- wos:000327374200014
- ISSN
- 1461-7285
- language
- English
- LU publication?
- yes
- id
- 86d9f01b-9bf6-417a-a6bd-96e5dee9b4c7 (old id 4275397)
- date added to LUP
- 2016-04-01 10:05:54
- date last changed
- 2018-11-21 19:41:04
@article{86d9f01b-9bf6-417a-a6bd-96e5dee9b4c7,
abstract = {{Glycan utilization plays a key role in modulating the composition of the gut microbiota, but molecular insight into oligosaccharide uptake by this microbial community is lacking. Arabinoxylo-oligosaccharides (AXOS) are abundant in the diet, and are selectively fermented by probiotic bifidobacteria in the colon. Here we show how selectivity for AXOS uptake is established by the probiotic strain Bifidobacterium animalis subsp. lactisBl-04. The binding protein BlAXBP, which is associated with an ATP-binding cassette (ABC) transporter that mediates the uptake of AXOS, displays an exceptionally broad specificity for arabinosyl-decorated and undecorated xylo-oligosaccharides, with preference for tri- and tetra-saccharides. Crystal structures of BlAXBP in complex with four different ligands revealed the basis for this versatility. Uniquely, the protein was able to recognize oligosaccharides in two opposite orientations, which facilitates the optimization of interactions with the various ligands. Broad substrate specificity was further enhanced by a spacious binding pocket accommodating decorations at different mainchain positions and conformational flexibility of a lid-like loop. Phylogenetic and genetic analyses show that BlAXBP is highly conserved within Bifidobacterium, but is lacking in other gut microbiota members. These data indicate niche adaptation within Bifidobacterium and highlight the metabolic syntrophy (cross-feeding) among the gut microbiota.}},
author = {{Ejby, Morten and Fredslund, Folmer and Vujicic-Zagar, Andreja and Svensson, Birte and Slotboom, Dirk Jan and Abou Hachem, Maher}},
issn = {{1461-7285}},
language = {{eng}},
number = {{11}},
pages = {{1100--1112}},
publisher = {{SAGE Publications}},
series = {{Journal of Psychopharmacology}},
title = {{Structural basis for arabinoxylo-oligosaccharide capture by the probiotic Bifidobacterium animalis subsp lactis Bl-04}},
volume = {{26}},
year = {{2012}},
}